HEADER LIGASE 06-MAR-06 2CGH
TITLE CRYSTAL STRUCTURE OF BIOTIN LIGASE FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIOTIN LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 6.3.4.15;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETM11
KEYWDS BIOTIN LIGASE, MYCOBACTERIUM TUBERCULOSIS, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.MA,M.WILMANNS
REVDAT 9 13-DEC-23 2CGH 1 REMARK
REVDAT 8 24-JUL-19 2CGH 1 REMARK
REVDAT 7 07-MAR-18 2CGH 1 SOURCE
REVDAT 6 12-JUL-17 2CGH 1
REVDAT 5 02-JUL-14 2CGH 1 JRNL
REVDAT 4 23-APR-14 2CGH 1 TITLE JRNL REMARK
REVDAT 3 13-JUL-11 2CGH 1 VERSN
REVDAT 2 24-FEB-09 2CGH 1 VERSN
REVDAT 1 01-MAY-07 2CGH 0
JRNL AUTH Q.MA,Y.AKHTER,M.WILMANNS,M.T.EHEBAUER
JRNL TITL ACTIVE SITE CONFORMATIONAL CHANGES UPON REACTION
JRNL TITL 2 INTERMEDIATE BIOTINYL-5'-AMP BINDING IN BIOTIN PROTEIN
JRNL TITL 3 LIGASE FROM MYCOBACTERIUM TUBERCULOSIS.
JRNL REF PROTEIN SCI. V. 23 932 2014
JRNL REFN ISSN 0961-8368
JRNL PMID 24723382
JRNL DOI 10.1002/PRO.2475
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45951
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2326
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3532
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3503
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 342
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 29.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.77000
REMARK 3 B22 (A**2) : 1.48000
REMARK 3 B33 (A**2) : -0.71000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.069
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3571 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3515 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4874 ; 1.775 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8047 ; 0.903 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 474 ;10.836 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 141 ;35.377 ;23.050
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 557 ;14.005 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;19.492 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 599 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4026 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 688 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 671 ; 0.217 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3539 ; 0.197 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1742 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2395 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 267 ; 0.172 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.126 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 74 ; 0.334 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.185 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2525 ; 1.178 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3784 ; 1.659 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1287 ; 2.590 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1090 ; 3.937 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 8 A 218
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2813 71.8882 14.0874
REMARK 3 T TENSOR
REMARK 3 T11: -0.0637 T22: -0.0731
REMARK 3 T33: -0.0830 T12: 0.0618
REMARK 3 T13: -0.0099 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 1.2434 L22: 1.8146
REMARK 3 L33: 3.5045 L12: 0.0948
REMARK 3 L13: 0.2976 L23: -1.0258
REMARK 3 S TENSOR
REMARK 3 S11: 0.0874 S12: 0.0710 S13: -0.0673
REMARK 3 S21: -0.2460 S22: -0.1340 S23: -0.1146
REMARK 3 S31: 0.2485 S32: 0.2173 S33: 0.0465
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 219 A 265
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6183 55.1238 32.2716
REMARK 3 T TENSOR
REMARK 3 T11: -0.0192 T22: -0.0576
REMARK 3 T33: -0.0776 T12: -0.0284
REMARK 3 T13: -0.0072 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 2.3119 L22: 3.4396
REMARK 3 L33: 2.3949 L12: 0.4550
REMARK 3 L13: 1.1396 L23: -2.0934
REMARK 3 S TENSOR
REMARK 3 S11: -0.0700 S12: 0.2459 S13: -0.1021
REMARK 3 S21: -0.2696 S22: 0.0604 S23: 0.0557
REMARK 3 S31: 0.0610 S32: -0.0890 S33: 0.0096
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 8 B 218
REMARK 3 ORIGIN FOR THE GROUP (A): 41.1501 55.6113 64.9394
REMARK 3 T TENSOR
REMARK 3 T11: -0.0863 T22: -0.0179
REMARK 3 T33: -0.0588 T12: 0.0400
REMARK 3 T13: 0.0095 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 2.0885 L22: 0.9064
REMARK 3 L33: 2.2059 L12: 0.1076
REMARK 3 L13: -0.5563 L23: -0.3695
REMARK 3 S TENSOR
REMARK 3 S11: -0.0948 S12: -0.4103 S13: -0.1564
REMARK 3 S21: 0.0392 S22: 0.0242 S23: 0.0935
REMARK 3 S31: 0.1460 S32: 0.1862 S33: 0.0706
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 219 B 265
REMARK 3 ORIGIN FOR THE GROUP (A): 42.2549 50.0105 41.1266
REMARK 3 T TENSOR
REMARK 3 T11: -0.0182 T22: -0.0807
REMARK 3 T33: -0.0286 T12: 0.0120
REMARK 3 T13: 0.0067 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 1.3208 L22: 2.5121
REMARK 3 L33: 3.2685 L12: 0.6074
REMARK 3 L13: 0.5143 L23: 0.0847
REMARK 3 S TENSOR
REMARK 3 S11: -0.1312 S12: 0.1370 S13: -0.1414
REMARK 3 S21: 0.0227 S22: 0.0403 S23: -0.1464
REMARK 3 S31: -0.0059 S32: 0.0795 S33: 0.0909
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. RESIDUES WITH CLEAR ELECTRON DENSITY ARE MODELED.
REMARK 4
REMARK 4 2CGH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1290028037.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9364
REMARK 200 MONOCHROMATOR : FOCUSING DOUBLE SILICON
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48344
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 39.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 16.00
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CASPR
REMARK 200 STARTING MODEL: PDB ENTRY 1HXD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS HCL PH8.5, 0.2M
REMARK 280 TRIMETHYLAMINE N-OXIDE, 20%(W/V) MPEG 2000, PH 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 31.04950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.94050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.50350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.94050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.04950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.50350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 ARG A 4
REMARK 465 ASP A 5
REMARK 465 ARG A 6
REMARK 465 LEU A 7
REMARK 465 ALA A 65
REMARK 465 GLY A 66
REMARK 465 ARG A 67
REMARK 465 GLY A 68
REMARK 465 ARG A 69
REMARK 465 HIS A 70
REMARK 465 GLY A 71
REMARK 465 ARG A 72
REMARK 465 GLY A 73
REMARK 465 TRP A 74
REMARK 465 ALA A 75
REMARK 465 ALA A 76
REMARK 465 ALA A 162
REMARK 465 PRO A 163
REMARK 465 GLU A 164
REMARK 465 GLU A 165
REMARK 465 VAL A 166
REMARK 465 ASP A 167
REMARK 465 PRO A 168
REMARK 465 ASP A 169
REMARK 465 ARG A 266
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ASP B 3
REMARK 465 ARG B 4
REMARK 465 ASP B 5
REMARK 465 ARG B 6
REMARK 465 LEU B 7
REMARK 465 GLY B 66
REMARK 465 ARG B 67
REMARK 465 GLY B 68
REMARK 465 ARG B 69
REMARK 465 HIS B 70
REMARK 465 GLY B 71
REMARK 465 ARG B 72
REMARK 465 GLY B 73
REMARK 465 TRP B 74
REMARK 465 ALA B 75
REMARK 465 ALA B 76
REMARK 465 PRO B 163
REMARK 465 GLU B 164
REMARK 465 GLU B 165
REMARK 465 VAL B 166
REMARK 465 ASP B 167
REMARK 465 ARG B 266
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 14 CD NE CZ NH1 NH2
REMARK 470 GLN A 35 CG CD OE1 NE2
REMARK 470 ARG A 89 NE CZ NH1 NH2
REMARK 470 GLU A 123 CG CD OE1 OE2
REMARK 470 ARG A 135 CD NE CZ NH1 NH2
REMARK 470 GLN A 161 CG CD OE1 NE2
REMARK 470 ARG B 14 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 135 NE CZ NH1 NH2
REMARK 470 GLN B 161 CG CD OE1 NE2
REMARK 470 ASP B 169 CB CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2131 O HOH B 2100 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP B 100 CB TRP B 100 CG -0.121
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 183 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 215 NE - CZ - NH1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 215 NE - CZ - NH2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 238 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP B 111 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LEU B 176 N - CA - C ANGL. DEV. = 24.3 DEGREES
REMARK 500 GLY B 177 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 ARG B 238 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 238 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 23 -69.10 -25.82
REMARK 500 ALA A 118 54.54 -95.50
REMARK 500 ALA A 122 -32.69 -25.38
REMARK 500 GLU A 123 -14.02 -145.92
REMARK 500 VAL A 159 -61.80 -99.62
REMARK 500 ALA B 23 132.21 -38.30
REMARK 500 ALA B 118 41.93 -89.83
REMARK 500 LEU B 176 -5.36 -52.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 122 GLU A 123 -104.72
REMARK 500 ASP B 175 LEU B 176 107.40
REMARK 500 LEU B 176 GLY B 177 130.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2008 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH B2024 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH B2051 DISTANCE = 6.18 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 OWING TO PLASMID CONSTRUCTION, THE SECOND AMINO ACID IS
REMARK 999 CHANGED FROM THR TO ALA. AND GLY AND ALA ARE ADDED TO THE
REMARK 999 N-TERMINAL OF THE PROTEIN.
DBREF 2CGH A -1 0 PDB 2CGH 2CGH -1 0
DBREF 2CGH A 1 266 UNP P96884 P96884_MYCTU 1 266
DBREF 2CGH B -1 0 PDB 2CGH 2CGH -1 0
DBREF 2CGH B 1 266 UNP P96884 P96884_MYCTU 1 266
SEQRES 1 A 268 GLY ALA MET ALA ASP ARG ASP ARG LEU ARG PRO PRO LEU
SEQRES 2 A 268 ASP GLU ARG SER LEU ARG ASP GLN LEU ILE GLY ALA GLY
SEQRES 3 A 268 SER GLY TRP ARG GLN LEU ASP VAL VAL ALA GLN THR GLY
SEQRES 4 A 268 SER THR ASN ALA ASP LEU LEU ALA ARG ALA ALA SER GLY
SEQRES 5 A 268 ALA ASP ILE ASP GLY VAL VAL LEU ILE ALA GLU HIS GLN
SEQRES 6 A 268 THR ALA GLY ARG GLY ARG HIS GLY ARG GLY TRP ALA ALA
SEQRES 7 A 268 THR ALA ARG ALA GLN ILE ILE LEU SER VAL GLY VAL ARG
SEQRES 8 A 268 VAL VAL ASP VAL PRO VAL GLN ALA TRP GLY TRP LEU SER
SEQRES 9 A 268 LEU ALA ALA GLY LEU ALA VAL LEU ASP SER VAL ALA PRO
SEQRES 10 A 268 LEU ILE ALA VAL PRO PRO ALA GLU THR GLY LEU LYS TRP
SEQRES 11 A 268 PRO ASN ASP VAL LEU ALA ARG GLY GLY LYS LEU ALA GLY
SEQRES 12 A 268 ILE LEU ALA GLU VAL ALA GLN PRO PHE VAL VAL LEU GLY
SEQRES 13 A 268 VAL GLY LEU ASN VAL THR GLN ALA PRO GLU GLU VAL ASP
SEQRES 14 A 268 PRO ASP ALA THR SER LEU LEU ASP LEU GLY VAL ALA ALA
SEQRES 15 A 268 PRO ASP ARG ASN ARG ILE ALA SER ARG LEU LEU ARG GLU
SEQRES 16 A 268 LEU GLU ALA ARG ILE ILE GLN TRP ARG ASN ALA ASN PRO
SEQRES 17 A 268 GLN LEU ALA ALA ASP TYR ARG ALA ARG SER LEU THR ILE
SEQRES 18 A 268 GLY SER ARG VAL ARG VAL GLU LEU PRO GLY GLY GLN ASP
SEQRES 19 A 268 VAL VAL GLY ILE ALA ARG ASP ILE ASP ASP GLN GLY ARG
SEQRES 20 A 268 LEU CYS LEU ASP VAL GLY GLY ARG THR VAL VAL VAL SER
SEQRES 21 A 268 ALA GLY ASP VAL VAL HIS LEU ARG
SEQRES 1 B 268 GLY ALA MET ALA ASP ARG ASP ARG LEU ARG PRO PRO LEU
SEQRES 2 B 268 ASP GLU ARG SER LEU ARG ASP GLN LEU ILE GLY ALA GLY
SEQRES 3 B 268 SER GLY TRP ARG GLN LEU ASP VAL VAL ALA GLN THR GLY
SEQRES 4 B 268 SER THR ASN ALA ASP LEU LEU ALA ARG ALA ALA SER GLY
SEQRES 5 B 268 ALA ASP ILE ASP GLY VAL VAL LEU ILE ALA GLU HIS GLN
SEQRES 6 B 268 THR ALA GLY ARG GLY ARG HIS GLY ARG GLY TRP ALA ALA
SEQRES 7 B 268 THR ALA ARG ALA GLN ILE ILE LEU SER VAL GLY VAL ARG
SEQRES 8 B 268 VAL VAL ASP VAL PRO VAL GLN ALA TRP GLY TRP LEU SER
SEQRES 9 B 268 LEU ALA ALA GLY LEU ALA VAL LEU ASP SER VAL ALA PRO
SEQRES 10 B 268 LEU ILE ALA VAL PRO PRO ALA GLU THR GLY LEU LYS TRP
SEQRES 11 B 268 PRO ASN ASP VAL LEU ALA ARG GLY GLY LYS LEU ALA GLY
SEQRES 12 B 268 ILE LEU ALA GLU VAL ALA GLN PRO PHE VAL VAL LEU GLY
SEQRES 13 B 268 VAL GLY LEU ASN VAL THR GLN ALA PRO GLU GLU VAL ASP
SEQRES 14 B 268 PRO ASP ALA THR SER LEU LEU ASP LEU GLY VAL ALA ALA
SEQRES 15 B 268 PRO ASP ARG ASN ARG ILE ALA SER ARG LEU LEU ARG GLU
SEQRES 16 B 268 LEU GLU ALA ARG ILE ILE GLN TRP ARG ASN ALA ASN PRO
SEQRES 17 B 268 GLN LEU ALA ALA ASP TYR ARG ALA ARG SER LEU THR ILE
SEQRES 18 B 268 GLY SER ARG VAL ARG VAL GLU LEU PRO GLY GLY GLN ASP
SEQRES 19 B 268 VAL VAL GLY ILE ALA ARG ASP ILE ASP ASP GLN GLY ARG
SEQRES 20 B 268 LEU CYS LEU ASP VAL GLY GLY ARG THR VAL VAL VAL SER
SEQRES 21 B 268 ALA GLY ASP VAL VAL HIS LEU ARG
FORMUL 3 HOH *342(H2 O)
HELIX 1 1 ASP A 12 ILE A 21 1 10
HELIX 2 2 SER A 38 SER A 49 1 12
HELIX 3 3 PRO A 94 TRP A 98 5 5
HELIX 4 4 GLY A 99 ALA A 114 1 16
HELIX 5 5 PRO A 115 ILE A 117 5 3
HELIX 6 6 PRO A 120 ALA A 122 5 3
HELIX 7 7 LEU A 173 GLY A 177 5 5
HELIX 8 8 ASP A 182 ASN A 203 1 22
HELIX 9 9 ASN A 205 ARG A 215 1 11
HELIX 10 10 ASP B 12 ILE B 21 1 10
HELIX 11 11 SER B 38 SER B 49 1 12
HELIX 12 12 PRO B 94 TRP B 98 5 5
HELIX 13 13 GLY B 99 ALA B 114 1 16
HELIX 14 14 PRO B 115 ILE B 117 5 3
HELIX 15 15 PRO B 120 ALA B 122 5 3
HELIX 16 16 SER B 172 GLY B 177 1 6
HELIX 17 17 ASP B 182 ASN B 203 1 22
HELIX 18 18 ASN B 205 SER B 216 1 12
SHEET 1 AA 7 GLN A 29 VAL A 33 0
SHEET 2 AA 7 VAL A 56 ALA A 60 1 O VAL A 57 N ASP A 31
SHEET 3 AA 7 GLN A 81 ARG A 89 -1 O ILE A 83 N ALA A 60
SHEET 4 AA 7 PHE A 150 ASN A 158 -1 O VAL A 151 N VAL A 88
SHEET 5 AA 7 GLY A 137 ALA A 147 -1 O LEU A 139 N ASN A 158
SHEET 6 AA 7 ASP A 131 ALA A 134 -1 O VAL A 132 N LEU A 139
SHEET 7 AA 7 THR A 124 LYS A 127 -1 O GLY A 125 N LEU A 133
SHEET 1 AB10 VAL A 263 LEU A 265 0
SHEET 2 AB10 ARG A 222 LEU A 227 -1 O ARG A 222 N LEU A 265
SHEET 3 AB10 GLN A 231 ILE A 240 -1 O GLN A 231 N LEU A 227
SHEET 4 AB10 LEU A 246 VAL A 250 -1 O CYS A 247 N ARG A 238
SHEET 5 AB10 ARG A 253 VAL A 257 -1 O ARG A 253 N VAL A 250
SHEET 6 AB10 ARG B 253 VAL B 257 -1 O VAL B 256 N VAL A 256
SHEET 7 AB10 LEU B 246 VAL B 250 -1 O LEU B 246 N VAL B 257
SHEET 8 AB10 GLN B 231 ILE B 240 -1 O ILE B 236 N ASP B 249
SHEET 9 AB10 ARG B 222 LEU B 227 -1 O VAL B 223 N GLY B 235
SHEET 10 AB10 VAL B 262 HIS B 264 -1 O VAL B 263 N ARG B 224
SHEET 1 BA 7 GLN B 29 VAL B 33 0
SHEET 2 BA 7 VAL B 56 ALA B 60 1 O VAL B 57 N ASP B 31
SHEET 3 BA 7 GLN B 81 ARG B 89 -1 O ILE B 83 N ALA B 60
SHEET 4 BA 7 PHE B 150 ASN B 158 -1 O VAL B 151 N VAL B 88
SHEET 5 BA 7 GLY B 137 ALA B 147 -1 O LEU B 139 N ASN B 158
SHEET 6 BA 7 ASP B 131 ALA B 134 -1 O VAL B 132 N LEU B 139
SHEET 7 BA 7 THR B 124 LYS B 127 -1 O GLY B 125 N LEU B 133
CISPEP 1 TRP A 128 PRO A 129 0 -2.65
CISPEP 2 GLN A 148 PRO A 149 0 6.87
CISPEP 3 TRP B 128 PRO B 129 0 -5.75
CISPEP 4 GLN B 148 PRO B 149 0 17.52
CRYST1 62.099 81.007 101.881 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016103 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012345 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009815 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
